| Autor: |
Xiaoyi Shi, Jiaran Geng, Jingxian Feng, Yingbo Yang, Xueqi Ma, Wansheng Chen, Ying Xiao |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Frontiers in Plant Science, Vol 13 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
1664-462X |
| DOI: |
10.3389/fpls.2022.1035121 |
| Popis: |
Cofactors are crucial for the biosynthesis of natural compounds, and cofactor engineering is a useful strategy for enzyme optimization due to its potential to enhance enzyme efficiency. Secoisolariciresinol dehydrogenase (SIRD) was reported to convert secoisolariciresinol into matairesinol in an NAD+-dependent reaction. Here, a SIRD designated as IiSIRD2 identified from Isatis indigotica was found to utilize NADP+ as the cofactor. To explore the structural basis for this unique cofactor preference, model-based structural analysis was carried out, and it was postulated that a variation at the GXGGXG glycine-rich motif of IiSIRD2 alters its cofactor preference. This study paves way for future investigations on SIRD cofactor specificity and cofactor engineering to improve SIRD’s catalytic efficiency. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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